DHHC9-mediated GLUT1 S-palmitoylation promotes glioblastoma glycolysis and tumorigenesis

Zhenxing Zhang, Xin Li, Fan Yang, Chao Chen, Ping Liu, Yi Ren, Pengkai Sun, Zixiong Wang, Yongping You, Yi-Xin Zeng and Xinjian Li ()
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Zhenxing Zhang: Chinese Academy of Sciences
Xin Li: Chinese Academy of Sciences
Fan Yang: Chinese Academy of Sciences
Chao Chen: Chinese Academy of Sciences
Ping Liu: Chinese Academy of Sciences
Yi Ren: Chinese Academy of Sciences
Pengkai Sun: Chinese Academy of Sciences
Zixiong Wang: Chinese Academy of Sciences
Yongping You: The First Affiliated Hospital of Nanjing Medical University
Yi-Xin Zeng: Chinese Academy of Sciences
Xinjian Li: Chinese Academy of Sciences

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Glucose transporter GLUT1 is a transmembrane protein responsible for the uptake of glucose into the cells of many tissues through facilitative diffusion. Plasma membrane (PM) localization is essential for glucose uptake by GLUT1. However, the mechanism underlying GLUT1 PM localization remains enigmatic. We find that GLUT1 is palmitoylated at Cys207, and S-palmitoylation is required for maintaining GLUT1 PM localization. Furthermore, we identify DHHC9 as the palmitoyl transferase responsible for this critical posttranslational modification. Knockout of DHHC9 or mutation of GLUT1 Cys207 to serine abrogates palmitoylation and PM distribution of GLUT1, and impairs glycolysis, cell proliferation, and glioblastoma (GBM) tumorigenesis. In addition, DHHC9 expression positively correlates with GLUT1 PM localization in GBM specimens and indicates a poor prognosis in GBM patients. These findings underscore that DHHC9-mediated GLUT1 S-palmitoylation is critical for glucose supply during GBM tumorigenesis.

Date: 2021
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DOI: 10.1038/s41467-021-26180-4

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